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FLASH GENE
Symbol PSTPIP1 contributors: mct - updated : 09-04-2015
HGNC name proline-serine-threonine phosphatase interacting protein 1
HGNC id 9580
EXPRESSION
Type
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Lymphoid/Immunespleen   highly
 thymus   highly
Nervousbrain   lowly
Reproductivemale systemtestis  lowly
Respiratorylung   lowly
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Blood / hematopoietic     Homo sapiens
Connectiveadipose  moderately
Lymphoid    
cells
SystemCellPubmedSpeciesStageRna symbol
Blood/Hematopoieticgranulocyte Homo sapiens
Blood/Hematopoieticmonocyte Homo sapiens
Blood/HematopoieticNK cell
cell lineage restricted to hemopoietic cells
cell lines
fluid/secretion highly in blood
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • N-terminal FER/CIP4 homologous domain (FCH),
  • an intermediate coiled coil domain mediating interaction with PTPN18, PTPN12 and CD2AP
  • an helical domain, variable length intervening PEST sequence
  • a C terminal SH3 domain mediating interaction with WAS and ABL1
  • a F-BAR domain
  • the SH3 and coiled-coil domains are necessary for the interaction with MEFV, and SH3 is implicated in its function
  • conjugated PhosphoP
    mono polymer homomer , trimer
    HOMOLOGY
    interspecies homolog to rattus Pstpip1 (86.1 pc)
    homolog to murine Pstpip1 (88.2 pc)
    Homologene
    FAMILY
    CATEGORY adhesion
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,cytosolic
    intracellular,cytoplasm,cytoskeleton
    text
  • cell projection, lamellipodium
  • perinuclear region
  • basic FUNCTION
  • acting as a CD2 tail binding protein
  • involved in the control processes for cell adhesion
  • involved in regulation of the actin cytoskeleton
  • may regulate the WAS actin-bundling activity
  • bridging the interaction between ABL1 and PTPN18 leading to the ABL1 dephosphorylation
  • may play a role as a scaffold protein between PTPN12 and WAS and allows PTPN12 to dephosphorylate WAS
  • having the potential to physically couple CD2 and CD2AP to WAS
  • acting downstream of CD2 and CD2AP to recruit WAS to the T-cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation
  • down-regulating CD2-stimulated adhesion through the coupling of PTPN12 to CD2
  • is not an essential regulator of the major types of caspase-1-activating inflammasomes, nor is it a critical regulator of the caspase-1 independent turpentine-induced inflammatory pathway 2)
  • cytoskeletal adaptor and F-BAR protein that has been implicated in autoinflammatory disease, most notably in the PAPA syndrome
  • endogenous PSTPIP1 negatively regulates macrophage podosome organization and matrix degradation
  • novel role for PSTPIP1 and WAS in orchestrating different
  • types of actin-based protrusions
  • adaptor protein associated with the cytoskeleton that is mainly expressed in hematopoietic cells
  • CELLULAR PROCESS cell communication
    PHYSIOLOGICAL PROCESS
    text control processes
    PATHWAY
    metabolism
    signaling signal transduction
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • pyrin binding
  • interacting with PTPN18, ABL1, CD2AP and WAS
  • interacting with CD2, PTPN12 and MEFV/pyrin
  • links PEST-type phosphatases to their substrates
  • interacts with PYRIN, the protein encoded by the Mediterranean Fever (MEFV) gene whose mutations cause Familial Mediterranean Fever (FMF)
  • interacts with PEST-type protein tyrosine phosphatases (PEST-PTPs)
  • cell & other
    REGULATION
    Other phosphorylation regulates the interaction with WAS and with MEFV
    ASSOCIATED DISORDERS
    corresponding disease(s) PSAPG
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
  • in the absence of Pstpip1 proteins, mouse macrophages responded normally to stimuli that activate the Nlrp3, Nlrc4, and Aim2 inflammasomes 2)